QM/MM modeling of compound I active species in cytochrome P450, cytochrome C peroxidase, and ascorbate peroxidase
نویسندگان
چکیده
منابع مشابه
Energetics of Cation Radical Formation at the Proximal Active Site Tryptophan of Cytochrome-c-Peroxidase and Ascorbate Peroxidase
Despite very similar protein structures, ascorbate peroxidase (APX) and yeast cytochrome-cperoxidase (CCP) stabilize different radical species during enzyme turnover. Both enzymes contain similar active site residues, including the tryptophan that is oxidized to a stable cation radical in CCP. However, the analogous trytophan is not oxidized in APX, and the second oxidizing equivalent is retain...
متن کاملStudies on Cytochrome c Peroxidase
Apoproteins of cytochrome c peroxidase, horseradish peroxidase, and sperm whale myoglobin were recombined with manganese complexes of proto-, hemato-, meso-, and deuteroporphyrins to form manganese porphyrin-protein complexes. These complexes were purified by column chromatography. All the manganese porphyrin-containing cytochrome c peroxidases were crystallized. Light absorption maxima of mang...
متن کاملHigh-resolution crystal structures and spectroscopy of native and compound I cytochrome c peroxidase.
Cytochrome c peroxidase (CCP) is a 32.5 kDa mitochondrial intermembrane space heme peroxidase from Saccharomyces cerevisiae that reduces H(2)O(2) to 2H(2)O by oxidizing two molecules of cytochrome c (cyt c). Here we compare the 1.2 A native structure (CCP) with the 1.3 A structure of its stable oxidized reaction intermediate, Compound I (CCP1). In addition, crystals were analyzed by UV-vis abso...
متن کاملThe crystal structure of cytochrome c peroxidase.
The three-dimensional conformation of yeast cytochrome c peroxidase has been determined from a 2.5 A electron density map computed with phases obtained from two isomorphous mercury derivatives. Partial sequence information that has recently become available aided in completion of the tracing of the polypeptide backbone, confirmed the presence of a proximal histidine heme ligand and aided in ide...
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Crystal structures of the complexes formed between cytochrome c peroxidase and cyanide, nitric oxide, carbon monoxide, apd fluoride have been determined and refined to 1.85 A. In all four complexes significant changes occur in the distal heme pocket due to movement of Arg-48, His-52, and a rearrangement of active site water molecules. In the cyanide, nitric oxide, and carbon monoxide complexes,...
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ژورنال
عنوان ژورنال: Journal of Computational Chemistry
سال: 2006
ISSN: 0192-8651,1096-987X
DOI: 10.1002/jcc.20446